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Conserved domains on  [gi|557440834|ref|NP_001273473|]
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cell cycle progression protein 1 isoform 3 [Mus musculus]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 289-519 3.75e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 3.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 289 ESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQI-RLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSF 367
Cdd:COG1196  252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELaRLEQDIARLEERRRELEERLEELEEELAELEEE 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 368 LREREMLLEEARMLKRDLEREQLTAMALRAELEqfipgQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLw 447
Cdd:COG1196  332 LEELEEELEELEEELEEAEEELEEAEAELAEAE-----EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL- 405

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557440834 448 erlyveAKDQHGKQETDGRKRGSRGSHRAKSKSKETFLGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKE 519
Cdd:COG1196  406 ------EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
PLN02328 super family cl33466
lysine-specific histone demethylase 1 homolog
 86-232 3.57e-04

lysine-specific histone demethylase 1 homolog


The actual alignment was detected with superfamily member PLN02328:

Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 44.21  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  86 EVEEAPSPEDNVYfGTTSDDSDI---VTLEPPKleemgnQEVTIQEAPSSDDLNMGSSSSSQYAFCQPE-----PVFSSQ 157
Cdd:PLN02328   4 ETKEPEDPADNVN-DVVSEASSPetdLSLSPSQ------SEQNIENDGQNSPETQSPLTELQPSPLPPNttldaPVSDSQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 158 PSDEES---SSDDTSHEPSPAPRRRRNRKKTVSiseseepplaepedEPSKEPS-KRHFSR-GLNKCVILALVIAVSMGF 232
Cdd:PLN02328  77 GDESSSeqqPQNPNSTEPAPPPKKRRRRKRFFT--------------EINANPAfRRHRVRgGLGKEVDVEALIAISVGF 142
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 289-519 3.75e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 3.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 289 ESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQI-RLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSF 367
Cdd:COG1196  252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELaRLEQDIARLEERRRELEERLEELEEELAELEEE 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 368 LREREMLLEEARMLKRDLEREQLTAMALRAELEqfipgQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLw 447
Cdd:COG1196  332 LEELEEELEELEEELEEAEEELEEAEAELAEAE-----EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL- 405

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557440834 448 erlyveAKDQHGKQETDGRKRGSRGSHRAKSKSKETFLGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKE 519
Cdd:COG1196  406 ------EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 297-449 1.29e-06

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 51.61  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  297 TQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVlkqyleVEKQKTDSFLREREMLLE 376
Cdd:pfam19220 132 EQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQA------AELAELTRRLAELETQLD 205

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557440834  377 EARMLKRDLEREQLTAMALRAELEqfipgqAQSRAESPSVQTEEKEVGL----LQQRLAELEQKLIfeQQRSDLWER 449
Cdd:pfam19220 206 ATRARLRALEGQLAAEQAERERAE------AQLEEAVEAHRAERASLRMkleaLTARAAATEQLLA--EARNQLRDR 274
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 261-530 2.35e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 2.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   261 LSQRKQEQESFLDFKSLKENLErcWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQ---EELRQLREQI-RL 336
Cdd:TIGR02169  203 LRREREKAERYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEkrlEEIEQLLEELnKK 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   337 LEDKGTSTQL-------------------VRENQVLKQYLEVEKQKTDSflrEREMLLEEARMLKRDLEREQLTAMALRA 397
Cdd:TIGR02169  281 IKDLGEEEQLrvkekigeleaeiaslersIAEKERELEDAEERLAKLEA---EIDKLLAEIEELEREIEEERKRRDKLTE 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   398 ELEQFIPGQAQSRAEspsVQTEEKEVGLLQQRLAELEQKLifeqqrSDLWERLYVEAKDQHGKQETDGRKRGSRGSHRAK 477
Cdd:TIGR02169  358 EYAELKEELEDLRAE---LEEVDKEFAETRDELKDYREKL------EKLKREINELKRELDRLQEELQRLSEELADLNAA 428

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 557440834   478 SKSKET----FLGTVKETFDAMKNSTKEF--VRHHKEKIKQAKEAVKENLKKFSDSVKS 530
Cdd:TIGR02169  429 IAGIEAkineLEEEKEDKALEIKKQEWKLeqLAADLSKYEQELYDLKEEYDRVEKELSK 487
PTZ00121 PTZ00121
MAEBL; Provisional
 264-601 4.08e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 4.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  264 RKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAEN-QYLRISLEKEEQALSSLQEELRQLR-EQIRLLED-K 340
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEaK 1619

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  341 GTSTQLVRENQV------LKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQLTAMALRAELEQfipgqaQSRAESP 414
Cdd:PTZ00121 1620 IKAEELKKAEEEkkkveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEA 1693

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  415 SVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERlYVEAKDQHGKQETDGRKrgsrgSHRAKSKSKETflgtvKETFDA 494
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN-KIKAEEAKKEAEEDKKK-----AEEAKKDEEEK-----KKIAHL 1762

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  495 MKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFD--EKGSKRFRAPKEAATEKTRTAYSYSSYS 572
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEggKEGNLVINDSKEMEDSAIKEVADSKNMQ 1842

                         330       340       350
                  ....*....|....*....|....*....|.
gi 557440834  573 QQEAP--NQNQNCRRPSAQRDGGREKPSHSE 601
Cdd:PTZ00121 1843 LEEADafEKHKFNKNNENGEDGNKEADFNKE 1873
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
 86-232 3.57e-04

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 44.21  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  86 EVEEAPSPEDNVYfGTTSDDSDI---VTLEPPKleemgnQEVTIQEAPSSDDLNMGSSSSSQYAFCQPE-----PVFSSQ 157
Cdd:PLN02328   4 ETKEPEDPADNVN-DVVSEASSPetdLSLSPSQ------SEQNIENDGQNSPETQSPLTELQPSPLPPNttldaPVSDSQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 158 PSDEES---SSDDTSHEPSPAPRRRRNRKKTVSiseseepplaepedEPSKEPS-KRHFSR-GLNKCVILALVIAVSMGF 232
Cdd:PLN02328  77 GDESSSeqqPQNPNSTEPAPPPKKRRRRKRFFT--------------EINANPAfRRHRVRgGLGKEVDVEALIAISVGF 142
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 289-519 3.75e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 3.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 289 ESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQI-RLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSF 367
Cdd:COG1196  252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELaRLEQDIARLEERRRELEERLEELEEELAELEEE 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 368 LREREMLLEEARMLKRDLEREQLTAMALRAELEqfipgQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLw 447
Cdd:COG1196  332 LEELEEELEELEEELEEAEEELEEAEAELAEAE-----EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL- 405

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557440834 448 erlyveAKDQHGKQETDGRKRGSRGSHRAKSKSKETFLGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKE 519
Cdd:COG1196  406 ------EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 252-457 3.74e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 3.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 252 DELDGVKGYLSQRKqeqESFLDFKSLKENLERCwtvtesEKITFEtQKKNLAaenqylriSLEKE-EQALS--SLQEELR 328
Cdd:COG1196  162 EEAAGISKYKERKE---EAERKLEATEENLERL------EDILGE-LERQLE--------PLERQaEKAERyrELKEELK 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 329 QLREQIRLLEDKGTSTQLVRENQVLKQyLEVEKQKTDSFLREREMLLEEARmLKRDLEREQLTAM-----ALRAELEQFI 403
Cdd:COG1196  224 ELEAELLLLKLRELEAELEELEAELEE-LEAELEELEAELAELEAELEELR-LELEELELELEEAqaeeyELLAELARLE 301

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 557440834 404 PGQAQSRAESPSVQTEEKEvglLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQ 457
Cdd:COG1196  302 QDIARLEERRRELEERLEE---LEEELAELEEELEELEEELEELEEELEEAEEE 352
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
275-437 6.67e-07

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 53.10  E-value: 6.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 275 KSLKENLercwTVTESEK-----ITFETQKKNLAAE------NQYLRISLEKE----EQALSSLQEELRQLREQIRLLED 339
Cdd:COG3206  121 ERLRKNL----TVEPVKGsnvieISYTSPDPELAAAvanalaEAYLEQNLELRreeaRKALEFLEEQLPELRKELEEAEA 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 340 KgtstqlvrenqvLKQYleveKQKTDSFLREREMLLEEARMlkRDLEREQLTAMALRAELEQFI----------PGQAQS 409
Cdd:COG3206  197 A------------LEEF----RQKNGLVDLSEEAKLLLQQL--SELESQLAEARAELAEAEARLaalraqlgsgPDALPE 258

                        170       180
                 ....*....|....*....|....*...
gi 557440834 410 RAESPSVQTEEKEVGLLQQRLAELEQKL 437
Cdd:COG3206  259 LLQSPVIQQLRAQLAELEAELAELSARY 286
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 297-449 1.29e-06

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 51.61  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  297 TQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVlkqyleVEKQKTDSFLREREMLLE 376
Cdd:pfam19220 132 EQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQA------AELAELTRRLAELETQLD 205

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557440834  377 EARMLKRDLEREQLTAMALRAELEqfipgqAQSRAESPSVQTEEKEVGL----LQQRLAELEQKLIfeQQRSDLWER 449
Cdd:pfam19220 206 ATRARLRALEGQLAAEQAERERAE------AQLEEAVEAHRAERASLRMkleaLTARAAATEQLLA--EARNQLRDR 274
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 261-530 2.35e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 2.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   261 LSQRKQEQESFLDFKSLKENLErcWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQ---EELRQLREQI-RL 336
Cdd:TIGR02169  203 LRREREKAERYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEkrlEEIEQLLEELnKK 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   337 LEDKGTSTQL-------------------VRENQVLKQYLEVEKQKTDSflrEREMLLEEARMLKRDLEREQLTAMALRA 397
Cdd:TIGR02169  281 IKDLGEEEQLrvkekigeleaeiaslersIAEKERELEDAEERLAKLEA---EIDKLLAEIEELEREIEEERKRRDKLTE 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   398 ELEQFIPGQAQSRAEspsVQTEEKEVGLLQQRLAELEQKLifeqqrSDLWERLYVEAKDQHGKQETDGRKRGSRGSHRAK 477
Cdd:TIGR02169  358 EYAELKEELEDLRAE---LEEVDKEFAETRDELKDYREKL------EKLKREINELKRELDRLQEELQRLSEELADLNAA 428

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 557440834   478 SKSKET----FLGTVKETFDAMKNSTKEF--VRHHKEKIKQAKEAVKENLKKFSDSVKS 530
Cdd:TIGR02169  429 IAGIEAkineLEEEKEDKALEIKKQEWKLeqLAADLSKYEQELYDLKEEYDRVEKELSK 487
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
298-457 1.19e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.00  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 298 QKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSfLREREMLLEE 377
Cdd:COG4717   82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE-LEERLEELRE 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 378 ARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEE--KEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAK 455
Cdd:COG4717  161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEElqQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240


                 ..
gi 557440834 456 DQ 457
Cdd:COG4717  241 LE 242
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 262-450 2.97e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 2.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   262 SQRKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKG 341
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   342 TSTQL-VRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQltamaLRAELEQFIPGQAQSRAESPSVQTEE 420
Cdd:TIGR02168  396 ASLNNeIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE-----LEEELEELQEELERLEEALEELREEL 470

                          170       180       190
                   ....*....|....*....|....*....|
gi 557440834   421 KEvglLQQRLAELEQKLIFEQQRSDLWERL 450
Cdd:TIGR02168  471 EE---AEQALDAAERELAQLQARLDSLERL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 260-533 3.40e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 3.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   260 YLSQRKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLED 339
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   340 KGTSTQ-----LVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLE-------REQLTAMALRAELEQFipgQA 407
Cdd:TIGR02168  825 RLESLErriaaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallneraSLEEALALLRSELEEL---SE 901

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   408 QSRAESPSVQTEEKEVGLLQQRLAELEQKLI-FEQQRSDLWERLYVEAKD--QHGKQETDGRKRGSRGSHR--AKSKSKE 482
Cdd:TIGR02168  902 ELRELESKRSELRRELEELREKLAQLELRLEgLEVRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEARRrlKRLENKI 981

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 557440834   483 TFLGTVkeTFDAM-----KNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFR 533
Cdd:TIGR02168  982 KELGPV--NLAAIeeyeeLKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
PTZ00121 PTZ00121
MAEBL; Provisional
 264-601 4.08e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 4.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  264 RKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAEN-QYLRISLEKEEQALSSLQEELRQLR-EQIRLLED-K 340
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEaK 1619

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  341 GTSTQLVRENQV------LKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQLTAMALRAELEQfipgqaQSRAESP 414
Cdd:PTZ00121 1620 IKAEELKKAEEEkkkveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEA 1693

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  415 SVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERlYVEAKDQHGKQETDGRKrgsrgSHRAKSKSKETflgtvKETFDA 494
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN-KIKAEEAKKEAEEDKKK-----AEEAKKDEEEK-----KKIAHL 1762

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  495 MKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFD--EKGSKRFRAPKEAATEKTRTAYSYSSYS 572
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEggKEGNLVINDSKEMEDSAIKEVADSKNMQ 1842

                         330       340       350
                  ....*....|....*....|....*....|.
gi 557440834  573 QQEAP--NQNQNCRRPSAQRDGGREKPSHSE 601
Cdd:PTZ00121 1843 LEEADafEKHKFNKNNENGEDGNKEADFNKE 1873
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 239-482 4.54e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.04  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  239 IQIQKQLVRKTHEDELDgvkgylsqrKQEQESFLDFKSLK-ENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEE 317
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE---------KMEQERLRQEKEEKaREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERER 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  318 QALSSLQEELRQLREQIRLlEDKGTSTQLVREnqvlKQYLEVEKQKTDSFLRERemlLEEARMLKRDLEREQLTAMALRA 397
Cdd:pfam17380 349 ELERIRQEERKRELERIRQ-EEIAMEISRMRE----LERLQMERQQKNERVRQE---LEAARKVKILEEERQRKIQQQKV 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  398 ELEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERlyveaKDQHGKQETDGRKRGSRGSHRAK 477
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER-----KRKKLELEKEKRDRKRAEEQRRK 495


                  ....*
gi 557440834  478 SKSKE 482
Cdd:pfam17380 496 ILEKE 500
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 240-446 5.51e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 5.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   240 QIQKQLVRKthEDELDGVKGYLSQRKQEQESFLDfkSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQA 319
Cdd:TIGR02169  241 AIERQLASL--EEELEKLTEEISELEKRLEEIEQ--LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   320 LSSLQEELRQLREQI-RLLEDKGTSTQLVRENQVLKQYLEVE-------------------------KQKTDSFLREREM 373
Cdd:TIGR02169  317 LEDAEERLAKLEAEIdKLLAEIEELEREIEEERKRRDKLTEEyaelkeeledlraeleevdkefaetRDELKDYREKLEK 396

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557440834   374 LLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEEKEvglLQQRLAELEQKLifEQQRSDL 446
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED---KALEIKKQEWKL--EQLAADL 464
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
252-426 7.78e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 7.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 252 DELDGVKGYLSQRKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKE--EQALSSLQEELRQ 329
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEalEAELAELPERLEE 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 330 LREQIRLLEDKGTS-TQLVRENQVLKQYLEVEKQKTD--------SFLREREMLLEEARMLKRDLEREQLTAMALRAELE 400
Cdd:COG4717  151 LEERLEELRELEEElEELEAELAELQEELEELLEQLSlateeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230

                        170       180
                 ....*....|....*....|....*.
gi 557440834 401 QFipgQAQSRAESPSVQTEEKEVGLL 426
Cdd:COG4717  231 QL---ENELEAAALEERLKEARLLLL 253
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
257-437 9.13e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.16  E-value: 9.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 257 VKGYLSQRKQEQESFLDF-----KSLKENLERcwtvTESEKITFETQKK--NLAAENQYLRISLEKEEQALSSLQEELRQ 329
Cdd:COG3206  162 LEQNLELRREEARKALEFleeqlPELRKELEE----AEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAE 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 330 LREQIRLLEDK----GTSTQLVRENQVLKQYLEvekqktdsflREREMLLEEARMLKRDLER--EQLTAMALRAELEQFI 403
Cdd:COG3206  238 AEARLAALRAQlgsgPDALPELLQSPVIQQLRA----------QLAELEAELAELSARYTPNhpDVIALRAQIAALRAQL 307

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 557440834 404 PGQAQSRAESPSVQTE--EKEVGLLQQRLAELEQKL 437
Cdd:COG3206  308 QQEAQRILASLEAELEalQAREASLQAQLAQLEARL 343
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 300-462 1.08e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   300 KNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKG--TSTQLVRENQVLKQYL-EVEK--QKTDSFLREREML 374
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELeeLSRQISALRKDLARLEaEVEQleERIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   375 LEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTE----EKEVGLLQQRLAELEQKLIFEQQRSDLWERL 450
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldelRAELTLLNEEAANLRERLESLERRIAATERR 839

                          170
                   ....*....|..
gi 557440834   451 YVEAKDQHGKQE 462
Cdd:TIGR02168  840 LEDLEEQIEELS 851
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
298-437 1.09e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  298 QKKNLAAENQYLR--ISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQlVRENQVLKQYLEVEKQKTDSFLREREMLL 375
Cdd:COG4913   266 AARERLAELEYLRaaLRLWFAQRRLELLEAELEELRAELARLEAELERLE-ARLDALREELDELEAQIRGNGGDRLEQLE 344

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557440834  376 EEARMLKRDLER---------EQLTAMALRAEL--EQFIPGQAQSRAESPSVQTEEKEvglLQQRLAELEQKL 437
Cdd:COG4913   345 REIERLERELEErerrrarleALLAALGLPLPAsaEEFAALRAEAAALLEALEEELEA---LEEALAEAEAAL 414
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 288-465 1.54e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 288 TESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDK--------------------------- 340
Cdd:COG4942   46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEleaqkeelaellralyrlgrqpplall 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 341 ---GTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEearmLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQ 417
Cdd:COG4942  126 lspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA----LRAELEAERAELEALLAELEEERAALEALKAERQKLL 201

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 557440834 418 TE-EKEVGLLQQRLAELEQKlifEQQRSDLWERLYVEAKDQHGKQETDG 465
Cdd:COG4942  202 ARlEKELAELAAELAELQQE---AEELEALIARLEAEAAAAAERTPAAG 247
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 313-531 2.19e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   313 LEKEEQALSSLQEELRQLREQIRLLEdkgtstqlvRENQVLKQYLEVEKQKTD-----------SFLREREMLLEEARML 381
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLE---------RQAEKAERYKELKAELRElelallvlrleELREELEELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   382 KRDLEREQLTAMALRAELEQFipgQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQhgkQ 461
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEEL---RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ---L 325

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   462 ETDGRKRGSRgshRAKSKSKETFLGTVKETFDAMKNSTKEFvRHHKEKIKQAKEAVKENLKKFSDSVKST 531
Cdd:TIGR02168  326 EELESKLDEL---AEELAELEEKLEELKEELESLEAELEEL-EAELEELESRLEELEEQLETLRSKVAQL 391
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 299-519 2.36e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   299 KKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTstQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEA 378
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE--QLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   379 RMLKRDLEREQLTAMALRAELE--------QFIPgqaQSRAESPSVqteEKEVGLLQQRLAELEQKLIFEQQRSDLWERL 450
Cdd:TIGR02169  761 KELEARIEELEEDLHKLEEALNdlearlshSRIP---EIQAELSKL---EEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557440834   451 YVEAKDQhgKQETDGRKRGSRGSHRAKSKSKETFLGTVKETFDAMKNSTKEF------VRHHKEKIKQAKEAVKE 519
Cdd:TIGR02169  835 IQELQEQ--RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlkkeRDELEAQLRELERKIEE 907
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 314-434 2.42e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 2.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 314 EKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQLTAM 393
Cdd:COG1196  661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 557440834 394 ALRAELEQFIPGqAQSRAESPSVQTEEKEVGLLQQRLAELE 434
Cdd:COG1196  741 LLEEEELLEEEA-LEELPEPPDLEELERELERLEREIEALG 780
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
296-462 2.61e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  296 ETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLED-KGTSTQLVRENQVLKQYLEVEKQ-----KTDSFLR 369
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIDVASAEREIAELEAElerldASSDDLA 688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  370 EREMLLEEARMLKRDLEREQLTAMALRAELEQFIPG------QAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQR 443
Cdd:COG4913   689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQaeeeldELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768

                         170
                  ....*....|....*....
gi 557440834  444 SDLWERLYVEAKDQHGKQE 462
Cdd:COG4913   769 ENLEERIDALRARLNRAEE 787
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 296-468 3.33e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 296 ETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDK--GTSTQLVRENQVLKQYLEVEKQKTDSFLREREM 373
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 374 LLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLifEQQRSDLwERLYVE 453
Cdd:COG4942  106 LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL--EAERAEL-EALLAE 182

                        170
                 ....*....|....*
gi 557440834 454 AKDQHGKQETDGRKR 468
Cdd:COG4942  183 LEEERAALEALKAER 197
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 253-446 3.37e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 44.12  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  253 ELDGVKGYLSQRKQEQESFLDfkSLKENLERCwtvtesekitfETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLRE 332
Cdd:pfam07888 133 ELEEDIKTLTQRVLERETELE--RMKERAKKA-----------GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRN 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  333 qirLLEDKGTSTQLVREN-QVLKQYLEVEKQKTdsflREREMLLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRA 411
Cdd:pfam07888 200 ---SLAQRDTQVLQLQDTiTTLTQKLTTAHRKE----AENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQA 272

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 557440834  412 E--SPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDL 446
Cdd:pfam07888 273 ElhQARLQAAQLTLQLADASLALREGRARWAQERETL 309
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
 86-232 3.57e-04

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 44.21  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  86 EVEEAPSPEDNVYfGTTSDDSDI---VTLEPPKleemgnQEVTIQEAPSSDDLNMGSSSSSQYAFCQPE-----PVFSSQ 157
Cdd:PLN02328   4 ETKEPEDPADNVN-DVVSEASSPetdLSLSPSQ------SEQNIENDGQNSPETQSPLTELQPSPLPPNttldaPVSDSQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 158 PSDEES---SSDDTSHEPSPAPRRRRNRKKTVSiseseepplaepedEPSKEPS-KRHFSR-GLNKCVILALVIAVSMGF 232
Cdd:PLN02328  77 GDESSSeqqPQNPNSTEPAPPPKKRRRRKRFFT--------------EINANPAfRRHRVRgGLGKEVDVEALIAISVGF 142
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 265-598 3.84e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 44.34  E-value: 3.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   265 KQEQESFL-DFKSLKENLErcwTVTESekitFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEdkGTS 343
Cdd:pfam15921  652 KQERDQLLnEVKTSRNELN---SLSED----YEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME--GSD 722

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   344 TQLVRENQVLKQYLEVEKQKTDS------FL--------REREMLLEEARMLKRDLEREQLTAMALRAELEQFipgQAQS 409
Cdd:pfam15921  723 GHAMKVAMGMQKQITAKRGQIDAlqskiqFLeeamtnanKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVL---RSQE 799

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   410 RAESPSVQTeeKEVGLLQQRLAELEQKLIFEQQrsdlwERLYVEAKDQHGKQETDGRKRGSRGSHRAKSKSKETFLGTVK 489
Cdd:pfam15921  800 RRLKEKVAN--MEVALDKASLQFAECQDIIQRQ-----EQESVRLKLQHTLDVKELQGPGYTSNSSMKPRLLQPASFTRT 872

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   490 ETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDEKG--------SKRFRAPKEAATEK 561
Cdd:pfam15921  873 HSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGrapslgalDDRVRDCIIESSLR 952

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 557440834   562 TRTAYSYSSYSQQEAPNQNQNC-RRPSAQRDGGREKPS 598
Cdd:pfam15921  953 SDICHSSSNSLQTEGSKSSETCsREPVLLHAGELEDPS 990
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
302-401 5.53e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 43.31  E-value: 5.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 302 LAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLED-----KGTSTQLVRENQVLKQYLEVEKQKTDSFLRER---EM 373
Cdd:COG2433  390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAeveelEAELEEKDERIERLERELSEARSEERREIRKDreiSR 469

                         90       100
                 ....*....|....*....|....*...
gi 557440834 374 LLEEARMLKRDLEREQLTAMALRAELEQ 401
Cdd:COG2433  470 LDREIERLERELEEERERIEELKRKLER 497
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
320-450 8.58e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 8.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  320 LSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMlkRDLEREQLTAMALRAEL 399
Cdd:COG4913   237 LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERL 314

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 557440834  400 EQFIpGQAQSRAESPSVQTEE---KEVGLLQQRLAELEQKLifeQQRSDLWERL 450
Cdd:COG4913   315 EARL-DALREELDELEAQIRGnggDRLEQLEREIERLEREL---EERERRRARL 364
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 253-455 9.26e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 9.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   253 ELDGVKGYLSQRKQEQEsflDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLRE 332
Cdd:TIGR02168  352 ELESLEAELEELEAELE---ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   333 QIRLLEDKGTSTQLVRENQVLKqylevEKQKTDSFLRERemlLEEARMLKRDLEREQLtamALRAELEqfipgQAQSRAE 412
Cdd:TIGR02168  429 KLEEAELKELQAELEELEEELE-----ELQEELERLEEA---LEELREELEEAEQALD---AAERELA-----QLQARLD 492

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 557440834   413 SPSVQTEEKEvGLLQQRLAELEQKLIFEQQRSDLWERLYVEAK 455
Cdd:TIGR02168  493 SLERLQENLE-GFSEGVKALLKNQSGLSGILGVLSELISVDEG 534
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
309-453 1.80e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 309 LRISLEKEEQALSSLQ--------EELRQLREQIRLLEDK-GTSTQLVRENQVLKQYLEvEKQKTDSFLREREMLLEEAR 379
Cdd:COG4717   47 LLERLEKEADELFKPQgrkpelnlKELKELEEELKEAEEKeEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLL 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557440834 380 MLKRDLEREQltamALRAELEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVE 453
Cdd:COG4717  126 QLLPLYQELE----ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
GvpP COG4980
Gas vesicle protein YhaH [General function prediction only];
488-545 1.95e-03

Gas vesicle protein YhaH [General function prediction only];


Pssm-ID: 444004 [Multi-domain]  Cd Length: 106  Bit Score: 38.41  E-value: 1.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 557440834 488 VKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDE 545
Cdd:COG4980   36 LKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEKIEELKEEVEPKIEE 93
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 290-441 2.29e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.90  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  290 SEKITFETQKKNLAAENQYLRISLEKEEqalSSLQEELRQLREQIRLLEDKgtstqlvrenqvlkqyLEVEKQKTDSFLR 369
Cdd:pfam09787  54 QERDLLREEIQKLRGQIQQLRTELQELE---AQQQEEAESSREQLQELEEQ----------------LATERSARREAEA 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557440834  370 EREMLLEEARMLKRDLEREQLTAMALRAELEQFI---PGQAQSRAESPSVQTEekevglLQQRLAELEQKLIFEQ 441
Cdd:pfam09787 115 ELERLQEELRYLEEELRRSKATLQSRIKDREAEIeklRNQLTSKSQSSSSQSE------LENRLHQLTETLIQKQ 183
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 310-437 2.34e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 310 RISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQ 389
Cdd:COG1196  662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 557440834 390 LTAMALRAELEQFIPGQAQSRAEspsvqteekevglLQQRLAELEQKL 437
Cdd:COG1196  742 LEEEELLEEEALEELPEPPDLEE-------------LERELERLEREI 776
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 289-450 3.59e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 289 ESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLE-DKGTSTQLVRENQvlKQYLEVEKQKT-DS 366
Cdd:COG1579   16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLElEIEEVEARIKKYE--EQLGNVRNNKEyEA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 367 FLREremlLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEEKEVglLQQRLAELEQKL-IFEQQRSD 445
Cdd:COG1579   94 LQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE--LDEELAELEAELeELEAEREE 167


                 ....*
gi 557440834 446 LWERL 450
Cdd:COG1579  168 LAAKI 172
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 288-446 4.35e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 40.49  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  288 TESEKITFETQKKNLAAENQYlrislEKEEQALSSLQEELRQLREqiRLLEDKGTSTQLVRENQVLKQYLEVEKQKtdsf 367
Cdd:pfam05557  23 LEHKRARIELEKKASALKRQL-----DRESDRNQELQKRIRLLEK--REAEAEEALREQAELNRLKKKYLEALNKK---- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834  368 LREREMLLEEARMLKRDLERE--QLTAMALRAELEqfipgqaqsraespsVQTEEKEVGLLQQRLAELEQKLI-FEQQRS 444
Cdd:pfam05557  92 LNEKESQLADAREVISCLKNElsELRRQIQRAELE---------------LQSTNSELEELQERLDLLKAKASeAEQLRQ 156


                  ..
gi 557440834  445 DL 446
Cdd:pfam05557 157 NL 158
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
240-552 4.72e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 240 QIQKQLVRKthEDELDGVKGYLSQRKQE-QESFLDFKSLKENLERcwtvTESEKITFETQKKNLAAENQYLRISLEKEEQ 318
Cdd:COG4372   63 QLEEELEQA--RSELEQLEEELEELNEQlQAAQAELAQAQEELES----LQEEAEELQEELEELQKERQDLEQQRKQLEA 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 319 ALSSLQEELRQLREQIRLLEDKGTSTQlvreNQVLKQYLEVEKQKTDSFLREREMLLEEARmlkRDLEREQLTAMALRAE 398
Cdd:COG4372  137 QIAELQSEIAEREEELKELEEQLESLQ----EELAALEQELQALSEAEAEQALDELLKEAN---RNAEKEEELAEAEKLI 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 399 LEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQHGKQETDGRKRGSRGSHRAKS 478
Cdd:COG4372  210 ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557440834 479 KSKETFLGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDEKGSKRFR 552
Cdd:COG4372  290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 314-534 5.80e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 5.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   314 EKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVReNQVLKQYLEVEKQKTDSFLREREM--LLEEARMLKRDLEREQLT 391
Cdd:TIGR02168  666 AKTNSSILERRREIEELEEKIEELEEKIAELEKAL-AELRKELEELEEELEQLRKELEELsrQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834   392 AMALRAELEQFIPGQAQSRAESPS-VQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQHGKQETDGRKRGS 470
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEErLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557440834   471 R-GSHRAKSKSKETFLGTVKETFDAMKNSTkEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRH 534
Cdd:TIGR02168  825 RlESLERRIAATERRLEDLEEQIEELSEDI-ESLAAEIEELEELIEELESELEALLNERASLEEA 888
DUF6627 pfam20332
Family of unknown function (DUF6627); This family of proteins is functionally uncharacterized. ...
 355-433 7.40e-03

Family of unknown function (DUF6627); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are approximately 130 amino acids in length.


Pssm-ID: 466482  Cd Length: 125  Bit Score: 37.51  E-value: 7.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557440834  355 QYLEVEKQKTDsflreREMLLEearMLKRDLEREQLTAMALRaeleqfiPGQAQSRAESPSVQteekEVGLLQQRLAEL 433
Cdd:pfam20332  29 QVIASEQAQVD-----RAQLLS---TLDRDDVQQQLTAMGVD-------PAQAAERVNRMTDQ----EVAQLNERLEDL 88
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
296-381 8.18e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 8.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440834 296 ETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTS-TQLVRENQVLKQYLEVEKQKTDSfLREREML 374
Cdd:COG2433  419 EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREiSRLDREIERLERELEEERERIEE-LKRKLER 497


                 ....*..
gi 557440834 375 LEEARML 381
Cdd:COG2433  498 LKELWKL 504
YtxH pfam12732
YtxH-like protein; This family of proteins is found in bacteria. Proteins in this family are ...
 476-529 9.07e-03

YtxH-like protein; This family of proteins is found in bacteria. Proteins in this family are typically between 100 and 143 amino acids in length. The N-terminal region is the most conserved. Proteins is this family are functionally uncharacterized.


Pssm-ID: 432750 [Multi-domain]  Cd Length: 71  Bit Score: 35.66  E-value: 9.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 557440834  476 AKSKSKETFlGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVK 529
Cdd:pfam12732  19 APKSGKETR-KDLKDKAEDLKDKAKDLAEEAKEKAEDLKEKVKEKADELKEKVK 71
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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